{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,26]],"date-time":"2026-10-26T12:29:53Z","timestamp":1793017793034,"version":"4.5.0"},"reference-count":143,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2025,11,25]],"date-time":"2025-11-25T00:00:00Z","timestamp":1764028800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0"},{"start":{"date-parts":[[2025,11,25]],"date-time":"2025-11-25T00:00:00Z","timestamp":1764028800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["J Transl Med"],"DOI":"10.1186\/s12967-025-07350-0","type":"journal-article","created":{"date-parts":[[2025,11,25]],"date-time":"2025-11-25T12:02:21Z","timestamp":1764072141000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":14,"title":["Histone modification\u2013mediated epigenetic regulation in AKI-to-CKD transition: a cell-type-specific perspective"],"prefix":"10.1186","volume":"23","author":[{"given":"Shouyu","family":"Chai","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhitao","family":"Zeng","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jiazhen","family":"Shang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yifan","family":"Xu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiaotian","family":"Han","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Baoze","family":"Ma","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5704-2151","authenticated-orcid":false,"given":"Zhimei","family":"Lv","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rong","family":"Wang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2025,11,25]]},"reference":[{"key":"7350_CR1","doi-asserted-by":"crossref","unstructured":"Al-Jaghbeer M, Dealmeida D, Bilderback A, Ambrosino R, Kellum JA. Clinical decision support for In-hospital aki. J Am Soc Nephrol. 2018;29(2):654\u201360.","DOI":"10.1681\/ASN.2017070765"},{"key":"7350_CR2","doi-asserted-by":"crossref","unstructured":"Singbartl K, Kellum JA. Aki in the icu: definition, epidemiology, risk stratification, and outcomes. Kidney Int. 2012;81(9):819\u201325.","DOI":"10.1038\/ki.2011.339"},{"key":"7350_CR3","doi-asserted-by":"crossref","unstructured":"Yeh TH, Tu KC, Wang HY, Chen JY. From acute to chronic: unraveling the pathophysiological mechanisms of the progression from acute kidney injury to acute kidney disease to chronic kidney disease. Int J Mol Sci. 2024;25(3).","DOI":"10.3390\/ijms25031755"},{"key":"7350_CR4","doi-asserted-by":"crossref","unstructured":"G\u00f3mez H, Kellum JA, Ronco C. Metabolic reprogramming and tolerance during sepsis-induced aki. Nat Rev Nephrol. 2017;13(3):143\u201351.","DOI":"10.1038\/nrneph.2016.186"},{"key":"7350_CR5","doi-asserted-by":"crossref","unstructured":"Yu SM, Bonventre JV. Acute kidney injury and maladaptive tubular repair leading to renal fibrosis. Curr Opin Nephrol Hypertens. 2020;29(3):310\u201318.","DOI":"10.1097\/MNH.0000000000000605"},{"key":"7350_CR6","doi-asserted-by":"crossref","unstructured":"Sato Y, Takahashi M, Yanagita M. Pathophysiology of aki to ckd progression. Semin Nephrol. 2020;40(2):206\u201315.","DOI":"10.1016\/j.semnephrol.2020.01.011"},{"key":"7350_CR7","doi-asserted-by":"crossref","unstructured":"Xu D, Zhang X, Pang J, Li Y, Peng Z. Mechanisms of acute kidney injury-chronic kidney disease transition: unraveling maladaptive repair and therapeutic opportunities. Biomolecules. 2025;15(6).","DOI":"10.3390\/biom15060794"},{"key":"7350_CR8","doi-asserted-by":"crossref","unstructured":"Ferenbach DA, Bonventre JV. Mechanisms of maladaptive repair after aki leading to accelerated kidney ageing and ckd. Nat Rev Nephrol. 2015;11(5):264\u201376.","DOI":"10.1038\/nrneph.2015.3"},{"key":"7350_CR9","doi-asserted-by":"crossref","unstructured":"Wang Z, Zhang C. From aki to ckd: maladaptive repair and the underlying mechanisms. Int J Mol Sci. 2022;23(18).","DOI":"10.3390\/ijms231810880"},{"key":"7350_CR10","doi-asserted-by":"crossref","unstructured":"Global. Regional, and national burden of chronic kidney disease, 1990-2017: a systematic analysis for the global burden of disease study 2017. Lancet. 2020;395(10225):709\u201333.","DOI":"10.1016\/S0140-6736(19)32977-0"},{"key":"7350_CR11","doi-asserted-by":"crossref","unstructured":"Yang L, Besschetnova TY, Brooks CR, Shah JV, Bonventre JV. Epithelial cell cycle arrest in G2\/M mediates kidney fibrosis after injury. Nat Med. 2010;16(5):535\u201343, 1p following 143.","DOI":"10.1038\/nm.2144"},{"key":"7350_CR12","doi-asserted-by":"crossref","unstructured":"Humphreys BD, Valerius MT, Kobayashi A, Mugford JW, Soeung S, Duffield JS, et al. Intrinsic epithelial cells repair the kidney after injury. Cell STEM Cell. 2008;2(3):284\u201391.","DOI":"10.1016\/j.stem.2008.01.014"},{"key":"7350_CR13","doi-asserted-by":"crossref","unstructured":"Basile DP. The endothelial cell in ischemic acute kidney injury: implications for acute and chronic function. Kidney Int. 2007;72(2):151\u201356.","DOI":"10.1038\/sj.ki.5002312"},{"key":"7350_CR14","doi-asserted-by":"crossref","unstructured":"Meng XM, Wang L, Nikolic-Paterson DJ, Lan HY. Innate immune cells in acute and chronic kidney disease. Nat Rev Nephrol. 2025;21(7):464\u201382.","DOI":"10.1038\/s41581-025-00958-x"},{"key":"7350_CR15","doi-asserted-by":"crossref","unstructured":"Guzzi F, Cirillo L, Roperto RM, Romagnani P, Lazzeri E. Molecular mechanisms of the acute kidney injury to chronic kidney disease transition: an updated view. Int J Mol Sci. 2019;20(19).","DOI":"10.3390\/ijms20194941"},{"key":"7350_CR16","doi-asserted-by":"crossref","unstructured":"Coca SG, Singanamala S, Parikh CR. Chronic kidney disease after acute kidney injury: a systematic review and meta-analysis. Kidney Int. 2012;81(5):442\u201348.","DOI":"10.1038\/ki.2011.379"},{"key":"7350_CR17","doi-asserted-by":"crossref","unstructured":"Tanemoto F, Nangaku M, Mimura I. Epigenetic memory contributing to the pathogenesis of AKI-to-CKD transition. Front Mol Biosci. 2022;9:1003227.","DOI":"10.3389\/fmolb.2022.1003227"},{"key":"7350_CR18","doi-asserted-by":"crossref","unstructured":"Mill\u00e1n-Zambrano G, Burton A, Bannister AJ, Schneider R. Histone post-translational modifications - cause and consequence of genome function. Nat Rev Genet. 2022;23(9):563\u201380.","DOI":"10.1038\/s41576-022-00468-7"},{"key":"7350_CR19","doi-asserted-by":"crossref","unstructured":"Liu R, Wu J, Guo H, Yao W, Li S, Lu Y, et al. Post-translational modifications of histones: mechanisms, biological functions, and therapeutic targets. MedComm. 2020). 2023;4(3):e292.","DOI":"10.1002\/mco2.292"},{"key":"7350_CR20","doi-asserted-by":"crossref","unstructured":"Bannister AJ, Kouzarides T. Regulation of chromatin by histone modifications. Cell Res. 2011;21(3):381\u201395.","DOI":"10.1038\/cr.2011.22"},{"issue":"5","key":"7350_CR21","doi-asserted-by":"publisher","first-page":"599","DOI":"10.1101\/gad.12.5.599","volume":"12","author":"K Struhl","year":"1998","unstructured":"Struhl K. Histone acetylation and transcriptional regulatory mechanisms. Genes Dev. 1998;12(5):599\u2013606.","journal-title":"Genes Dev"},{"issue":"4","key":"7350_CR22","doi-asserted-by":"publisher","first-page":"e324","DOI":"10.1038\/emm.2017.11","volume":"49","author":"K Hyun","year":"2017","unstructured":"Hyun K, Jeon J, Park K, Kim J. Writing, erasing and reading histone lysine methylations. Exp Mol Med. 2017;49(4):e324.","journal-title":"Exp Mol Med"},{"issue":"1","key":"7350_CR23","doi-asserted-by":"publisher","first-page":"58","DOI":"10.1056\/NEJMra1214243","volume":"371","author":"LS Chawla","year":"2014","unstructured":"Chawla LS, Eggers PW, Star RA, Kimmel PL. Acute kidney injury and chronic kidney disease as interconnected syndromes. N Engl J Med. 2014;371(1):58\u201366.","journal-title":"N Engl J Med"},{"issue":"4","key":"7350_CR24","doi-asserted-by":"publisher","first-page":"817","DOI":"10.1016\/j.ekir.2024.01.034","volume":"9","author":"SK Jensen","year":"2024","unstructured":"Jensen SK, Heide-J\u00f8rgensen U, Gammelager H, Birn H, Christiansen CF. Acute kidney injury duration and 20-year risks of CKD and Cardiovascular disease. Kidney Int Rep. 2024;9(4):817\u201329.","journal-title":"Kidney Int Rep"},{"issue":"1","key":"7350_CR25","doi-asserted-by":"publisher","first-page":"160","DOI":"10.1016\/j.kint.2018.08.036","volume":"95","author":"EJ See","year":"2019","unstructured":"See EJ, Jayasinghe K, Glassford N, Bailey M, Johnson DW, Polkinghorne KR, et al. Long-term risk of adverse outcomes after acute kidney injury: a systematic review and meta-analysis of cohort studies using consensus definitions of exposure. Kidney Int. 2019;95(1):160\u201372.","journal-title":"Kidney Int"},{"issue":"3","key":"7350_CR26","doi-asserted-by":"publisher","first-page":"552","DOI":"10.1016\/j.kint.2016.08.025","volume":"91","author":"L Gewin","year":"2017","unstructured":"Gewin L, Zent R, Pozzi A. Progression of chronic kidney disease: too much cellular talk causes damage. Kidney Int. 2017;91(3):552\u201360.","journal-title":"Kidney Int"},{"issue":"8","key":"7350_CR27","doi-asserted-by":"publisher","first-page":"1358","DOI":"10.1681\/ASN.2019040415","volume":"30","author":"L Chen","year":"2019","unstructured":"Chen L, Clark JZ, Nelson JW, Kaissling B, Ellison DH, Knepper MA. Renal-tubule epithelial cell nomenclature for single-cell RNA-Sequencing studies. J Am Soc Nephrol. 2019;30(8):1358\u201364.","journal-title":"J Am Soc Nephrol"},{"key":"7350_CR28","doi-asserted-by":"crossref","unstructured":"Baker ML, Cantley LG. Adding insult to injury: the spectrum of tubulointerstitial responses in acute kidney injury. J. Clin. Invest. 2025;135(6).","DOI":"10.1172\/JCI188358"},{"key":"7350_CR29","doi-asserted-by":"crossref","unstructured":"Lin Y, Yang Q, Zeng R. Crosstalk between macrophages and adjacent cells in aki to ckd transition. Ren Fail. 2025;47(1):2478482.","DOI":"10.1080\/0886022X.2025.2478482"},{"key":"7350_CR30","doi-asserted-by":"crossref","unstructured":"Wen Y, Yan HR, Wang B, Liu BC. Macrophage heterogeneity in kidney injury and fibrosis. Front Immunol. 2021;12:681748.","DOI":"10.3389\/fimmu.2021.681748"},{"key":"7350_CR31","doi-asserted-by":"publisher","first-page":"934299","DOI":"10.3389\/fimmu.2022.934299","volume":"13","author":"H Chen","year":"2022","unstructured":"Chen H, Liu N, Zhuang S. Macrophages in renal injury, repair, fibrosis following acute kidney injury and targeted therapy. Front Immunol. 2022;13:934299.","journal-title":"Front Immunol"},{"issue":"8","key":"7350_CR32","doi-asserted-by":"publisher","first-page":"2980","DOI":"10.7150\/ijbs.96812","volume":"20","author":"W Jiang","year":"2024","unstructured":"Jiang W, Tang TT, Zhang YL, Li ZL, Wen Y, Yang Q, et al. CD8 T cells induce the peritubular capillary rarefaction during aki to ckd transition. Int J Biol Sci. 2024;20(8):2980\u201393.","journal-title":"Int J Biol Sci"},{"key":"7350_CR33","doi-asserted-by":"crossref","unstructured":"Dellepiane S, Leventhal JS, Cravedi P. T cells and acute kidney injury: a two-way relationship. Front Immunol. 2020;11:1546.","DOI":"10.3389\/fimmu.2020.01546"},{"key":"7350_CR34","doi-asserted-by":"crossref","unstructured":"Wei K, Nguyen HN, Brenner MB. Fibroblast pathology in inflammatory diseases. J. Clin. Invest. 2021;131(20).","DOI":"10.1172\/JCI149538"},{"key":"7350_CR35","unstructured":"Ikuno Y, Kazlauskas A. TGFbeta1-dependent contraction of fibroblasts is mediated by the PDGFalpha receptor. Invest Ophthalmol Vis Sci. 2002;43(1):41\u201346."},{"key":"7350_CR36","doi-asserted-by":"crossref","unstructured":"Liu Y. Cellular and molecular mechanisms of renal fibrosis. Nat Rev Nephrol. 2011;7(12):684\u201396.","DOI":"10.1038\/nrneph.2011.149"},{"key":"7350_CR37","doi-asserted-by":"crossref","unstructured":"Di X, Chen J, Li Y, Wang M, Wei J, Li T, et al. Crosstalk between fibroblasts and immunocytes in fibrosis: from molecular mechanisms to clinical trials. Clin Transl Med. 2024;14(1):e1545.","DOI":"10.1002\/ctm2.1545"},{"key":"7350_CR38","doi-asserted-by":"crossref","unstructured":"Sutton TA, Fisher CJ, Molitoris BA. Microvascular endothelial injury and dysfunction during ischemic acute renal failure. Kidney Int. 2002;62(5):1539\u201349.","DOI":"10.1046\/j.1523-1755.2002.00631.x"},{"key":"7350_CR39","doi-asserted-by":"crossref","unstructured":"Czopek A, Moorhouse R, Gallacher PJ, Pugh D, Ivy JR, Farrah TE, et al. Endothelin blockade prevents the long-term cardiovascular and renal sequelae of acute kidney injury in mice. Sci Transl Med. 2022;14(675):eabf5074.","DOI":"10.1126\/scitranslmed.abf5074"},{"key":"7350_CR40","doi-asserted-by":"crossref","unstructured":"Kida Y. Peritubular Capillary Rarefaction: an underappreciated regulator of ckd progression. Int J Mol Sci. 2020;21(21).","DOI":"10.3390\/ijms21218255"},{"issue":"3","key":"7350_CR41","doi-asserted-by":"publisher","first-page":"295","DOI":"10.1093\/ckj\/sfx133","volume":"11","author":"B Afsar","year":"2018","unstructured":"Afsar B, Afsar RE, Dagel T, Kaya E, Erus S, Ortiz A, et al. Capillary rarefaction from the kidney point of view. Clin Kidney J. 2018;11(3):295\u2013301.","journal-title":"Clin Kidney J"},{"key":"7350_CR42","doi-asserted-by":"crossref","unstructured":"Niculae A, Gherghina ME, Peride I, Tiglis M, Nechita AM, Checherita IA. Pathway from acute kidney injury to chronic kidney disease: molecules involved in renal fibrosis. Int J Mol Sci. 2023;24(18).","DOI":"10.3390\/ijms241814019"},{"key":"7350_CR43","doi-asserted-by":"crossref","unstructured":"Jiang H, Shen Z, Zhuang J, Lu C, Qu Y, Xu C, et al. Understanding the podocyte immune responses in proteinuric kidney diseases: from pathogenesis to therapy. Front Immunol. 2023;14:1335936.","DOI":"10.3389\/fimmu.2023.1335936"},{"key":"7350_CR44","doi-asserted-by":"crossref","unstructured":"Hu S, Hang X, Wei Y, Wang H, Zhang L, Zhao L. Crosstalk among podocytes, glomerular endothelial cells and mesangial cells in diabetic kidney disease: an updated review. Cell Commun Signal. 2024;22(1):136.","DOI":"10.1186\/s12964-024-01502-3"},{"key":"7350_CR45","doi-asserted-by":"crossref","unstructured":"Chen SJ, Lv LL, Liu BC, Tang RN. Crosstalk between tubular epithelial cells and glomerular endothelial cells in diabetic kidney disease. Cell Prolif. 2020;53(3):e12763.","DOI":"10.1111\/cpr.12763"},{"key":"7350_CR46","doi-asserted-by":"crossref","unstructured":"Kornberg RD. Chromatin structure: a repeating unit of histones and dna. Science. 1974;184(4139):868\u201371.","DOI":"10.1126\/science.184.4139.868"},{"key":"7350_CR47","doi-asserted-by":"crossref","unstructured":"Luger K, M\u00e4der AW, Richmond RK, Sargent DF, Richmond TJ. Crystal structure of the nucleosome core particle at 2.8 a resolution. Nature. 1997;389(6648):251\u201360.","DOI":"10.1038\/38444"},{"key":"7350_CR48","doi-asserted-by":"crossref","unstructured":"Strahl BD, Allis CD. The language of covalent histone modifications. Nature. 2000;403(6765):41\u201345.","DOI":"10.1038\/47412"},{"key":"7350_CR49","doi-asserted-by":"crossref","unstructured":"Lawrence M, Daujat S, Schneider R. Lateral thinking: how histone modifications regulate gene expression. Trends Genet. 2016;32(1):42\u201356.","DOI":"10.1016\/j.tig.2015.10.007"},{"key":"7350_CR50","doi-asserted-by":"crossref","unstructured":"Black JC, Van Rechem C, Whetstine JR. Histone lysine methylation dynamics: establishment, regulation, and biological impact. Mol Cell. 2012;48(4):491\u2013507.","DOI":"10.1016\/j.molcel.2012.11.006"},{"key":"7350_CR51","doi-asserted-by":"crossref","unstructured":"Shvedunova M, Akhtar A. Modulation of cellular processes by histone and non-histone protein acetylation. Nat Rev Mol Cell Biol. 2022;23(5):329\u201349.","DOI":"10.1038\/s41580-021-00441-y"},{"key":"7350_CR52","doi-asserted-by":"crossref","unstructured":"Visan I. Histone lactylation. Nat Immunol. 2019;20(12):1558.","DOI":"10.1038\/s41590-019-0551-6"},{"key":"7350_CR53","doi-asserted-by":"crossref","unstructured":"Mattiroli F, Penengo L. Histone ubiquitination: an integrative signaling platform in genome stability. Trends Genet. 2021;37(6):566\u201381.","DOI":"10.1016\/j.tig.2020.12.005"},{"key":"7350_CR54","doi-asserted-by":"crossref","unstructured":"Li K, Wang Z. Histone crotonylation-centric gene regulation. Epigenet Chromatin. 2021;14(1):10.","DOI":"10.1186\/s13072-021-00385-9"},{"issue":"4","key":"7350_CR55","doi-asserted-by":"publisher","first-page":"214","DOI":"10.1016\/j.tig.2004.02.007","volume":"20","author":"SJ Nowak","year":"2004","unstructured":"Nowak SJ, Corces VG. Phosphorylation of histone H3: a balancing act between chromosome condensation and transcriptional activation. Trends Genet. 2004;20(4):214\u201320.","journal-title":"Trends Genet"},{"issue":"1","key":"7350_CR56","doi-asserted-by":"publisher","first-page":"232","DOI":"10.1038\/s41392-024-01918-w","volume":"9","author":"W Yao","year":"2024","unstructured":"Yao W, Hu X, Wang X. Crossing epigenetic frontiers: the intersection of novel histone modifications and diseases. Signal Transduct Target Ther. 2024;9(1):232.","journal-title":"Signal Transduct Target Ther"},{"issue":"2","key":"7350_CR57","doi-asserted-by":"publisher","first-page":"315","DOI":"10.1016\/j.cell.2006.02.041","volume":"125","author":"BE Bernstein","year":"2006","unstructured":"Bernstein BE, Mikkelsen TS, Xie X, Kamal M, Huebert DJ, Cuff J, et al. A bivalent chromatin structure marks key developmental genes in embryonic stem cells. Cell. 2006;125(2):315\u201326.","journal-title":"Cell"},{"issue":"1","key":"7350_CR58","doi-asserted-by":"publisher","first-page":"72","DOI":"10.1186\/s13148-024-01682-2","volume":"16","author":"Y Hu","year":"2024","unstructured":"Hu Y, He Z, Li Z, Wang Y, Wu N, Sun H, et al. Lactylation: the novel histone modification influence on gene expression, protein function, and disease. Clin Epigenet. 2024;16(1):72.","journal-title":"Clin Epigenet"},{"issue":"4","key":"7350_CR59","doi-asserted-by":"publisher","first-page":"564","DOI":"10.1038\/cr.2011.42","volume":"21","author":"M Yun","year":"2011","unstructured":"Yun M, Wu J, Workman JL, Li B. Readers of histone modifications. Cell Res. 2011;21(4):564\u201378.","journal-title":"Cell Res"},{"issue":"6","key":"7350_CR60","doi-asserted-by":"publisher","first-page":"1860","DOI":"10.7150\/thno.83353","volume":"13","author":"B Li","year":"2023","unstructured":"Li B, Xia Y, Mei S, Ye Z, Song B, Yan X, et al. Histone H3K27 methyltransferase EZH2 regulates apoptotic and inflammatory responses in sepsis-induced aki. Theranostics. 2023;13(6):1860\u201375.","journal-title":"Theranostics"},{"issue":"1","key":"7350_CR61","doi-asserted-by":"publisher","first-page":"147","DOI":"10.1038\/ki.2015.291","volume":"89","author":"T Irifuku","year":"2016","unstructured":"Irifuku T, Doi S, Sasaki K, Doi T, Nakashima A, Ueno T, et al. Inhibition of H3K9 histone methyltransferase G9a attenuates renal fibrosis and retains klotho expression. Kidney Int. 2016;89(1):147\u201357.","journal-title":"Kidney Int"},{"issue":"1","key":"7350_CR62","doi-asserted-by":"publisher","first-page":"483","DOI":"10.1172\/JCI95946","volume":"128","author":"S Majumder","year":"2018","unstructured":"Majumder S, Thieme K, Batchu SN, Alghamdi TA, Bowskill BB, Kabir MG, et al. Shifts in podocyte histone H3K27me3 regulate mouse and human glomerular disease. J. Clin. Invest. 2018;128(1):483\u201399.","journal-title":"J. Clin. Invest"},{"issue":"1","key":"7350_CR63","doi-asserted-by":"publisher","first-page":"2456418","DOI":"10.1080\/15592294.2025.2456418","volume":"20","author":"S Shaikh","year":"2025","unstructured":"Shaikh S, Zhao X, Wagner RT, Pan X, Hlady RA, Wang L, et al. Deciphering the interplay between SETD2 mediated H3K36me3 and rna N6-methyladenosine in clear cell renal cell carcinoma (ccRCC). Epigenetics. 2025;20(1):2456418.","journal-title":"Epigenetics"},{"issue":"6","key":"7350_CR64","doi-asserted-by":"publisher","first-page":"466","DOI":"10.1007\/s12272-019-01156-7","volume":"42","author":"JE Kim","year":"2019","unstructured":"Kim JE. Bookmarking by histone methylation ensures chromosomal integrity during mitosis. Arch. Pharm. Res. 2019;42(6):466\u201380.","journal-title":"Arch. Pharm. Res"},{"issue":"8","key":"7350_CR65","doi-asserted-by":"publisher","first-page":"454","DOI":"10.1038\/s41580-019-0157-8","volume":"20","author":"E Zlotorynski","year":"2019","unstructured":"Zlotorynski E. Histone methylation boosts liver regeneration. Nat Rev Mol Cell Biol. 2019;20(8):454\u201355.","journal-title":"Nat Rev Mol Cell Biol"},{"key":"7350_CR66","doi-asserted-by":"crossref","unstructured":"Marsolier J, Prompsy P, Durand A, Lyne AM, Landragin C, Trouchet A, et al. H3K27me3 conditions chemotolerance in triple-negative breast cancer. Nat Genet. 2022;54(4):459\u201368.","DOI":"10.1038\/s41588-022-01047-6"},{"key":"7350_CR67","doi-asserted-by":"crossref","unstructured":"Pan S, Yuan T, Xia Y, Yu W, Zhou X, Cheng F. Role of histone modifications in kidney fibrosis. Medicina (Kaunas). 2024;60(6).","DOI":"10.3390\/medicina60060888"},{"key":"7350_CR68","doi-asserted-by":"crossref","unstructured":"Liu H, Wang L, Weng X, Chen H, Du Y, Diao C, et al. Inhibition of Brd4 alleviates renal ischemia\/reperfusion injury-induced apoptosis and endoplasmic reticulum stress by blocking FoxO4-mediated oxidative stress. Redox Biol. 2019;24:101195.","DOI":"10.1016\/j.redox.2019.101195"},{"key":"7350_CR69","doi-asserted-by":"crossref","unstructured":"Zhang C, Xue S, Ren P, Han S, Zhou Y, Si Y, et al. Advances in the epigenetic mechanisms of diabetic nephropathy pathogenesis. Diabetes Metab Syndr Obes. 2025;18:2629\u201339.","DOI":"10.2147\/DMSO.S507171"},{"key":"7350_CR70","doi-asserted-by":"crossref","unstructured":"Wu CJ, Xu X, Yuan DY, Liu ZZ, Tan LM, Su YN, et al. Arabidopsis histone acetyltransferase complex coordinates cytoplasmic histone acetylation and nuclear chromatin accessibility. Sci Adv. 2024;10(49):eadp1840.","DOI":"10.1126\/sciadv.adp1840"},{"issue":"1","key":"7350_CR71","doi-asserted-by":"publisher","first-page":"47","DOI":"10.1186\/s13024-023-00625-4","volume":"18","author":"Y Lin","year":"2023","unstructured":"Lin Y, Lin A, Cai L, Huang W, Yan S, Wei Y, et al. ACSS2-dependent histone acetylation improves cognition in mouse model of Alzheimer\u2019s disease. Mol Neurodegener. 2023;18(1):47.","journal-title":"Mol Neurodegener"},{"issue":"23","key":"7350_CR72","doi-asserted-by":"publisher","first-page":"e2301094","DOI":"10.1002\/advs.202301094","volume":"10","author":"Y He","year":"2023","unstructured":"He Y, Wang S, Liu S, Qin D, Liu Z, Wang L, et al. MSL1 promotes liver regeneration by driving phase separation of STAT3 and histone H4 and enhancing their acetylation. Adv Sci (Weinh). 2023;10(23):e2301094.","journal-title":"Adv Sci (Weinh)"},{"issue":"1","key":"7350_CR73","doi-asserted-by":"publisher","first-page":"3200","DOI":"10.1038\/s41467-024-47315-3","volume":"15","author":"L Li","year":"2024","unstructured":"Li L, Xiang T, Guo J, Guo F, Wu Y, Feng H, et al. Inhibition of ACSS2-mediated histone crotonylation alleviates kidney fibrosis via IL-1\u03b2-dependent macrophage activation and tubular cell senescence. Nat Commun. 2024;15(1):3200.","journal-title":"Nat Commun"},{"key":"7350_CR74","doi-asserted-by":"crossref","unstructured":"Ruiz-Andres O, Sanchez-Ni\u00f1o MD, Cannata-Ortiz P, Ruiz-Ortega M, Egido J, Ortiz A, et al. Histone lysine crotonylation during acute kidney injury in mice. Dis Model Mech. 2016;9(6):633\u201345.","DOI":"10.1242\/dmm.024455"},{"key":"7350_CR75","doi-asserted-by":"crossref","unstructured":"He Y, Xie Y, Zhou T, Li D, Cheng X, Yang P, et al. Sodium crotonate alleviates diabetic kidney disease partially via the histone crotonylation pathway. Inflammation. 2025;48(1):254\u201375.","DOI":"10.1007\/s10753-024-02047-w"},{"key":"7350_CR76","doi-asserted-by":"crossref","unstructured":"Dang L, Cao X, Zhang T, Sun Y, Tian S, Gong T, et al. Nuclear condensation of CDYL links histone crotonylation and cystogenesis in autosomal dominant polycystic kidney disease. J Am Soc Nephrol. 2022;33(9):1708\u201325.","DOI":"10.1681\/ASN.2021111425"},{"key":"7350_CR77","doi-asserted-by":"crossref","unstructured":"Sabari BR, Tang Z, Huang H, Yong-Gonzalez V, Molina H, Kong HE, et al. Intracellular crotonyl-CoA stimulates transcription through p300-catalyzed histone crotonylation. Mol Cell. 2015;58(2):203\u201315.","DOI":"10.1016\/j.molcel.2015.02.029"},{"issue":"6","key":"7350_CR78","doi-asserted-by":"publisher","first-page":"1016","DOI":"10.1016\/j.cell.2011.08.008","volume":"146","author":"M Tan","year":"2011","unstructured":"Tan M, Luo H, Lee S, Jin F, Yang JS, Montellier E, et al. Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification. Cell. 2011;146(6):1016\u201328.","journal-title":"Cell"},{"issue":"1","key":"7350_CR79","doi-asserted-by":"publisher","first-page":"70","DOI":"10.1016\/j.stemcr.2018.05.003","volume":"11","author":"H Fu","year":"2018","unstructured":"Fu H, Tian CL, Ye X, Sheng X, Wang H, Liu Y, et al. Dynamics of telomere rejuvenation during chemical induction to pluripotent stem cells. STEM Cell Rep. 2018;11(1):70\u201387.","journal-title":"STEM Cell Rep"},{"issue":"2","key":"7350_CR80","doi-asserted-by":"publisher","first-page":"226","DOI":"10.1016\/j.kint.2024.04.016","volume":"106","author":"Y Wang","year":"2024","unstructured":"Wang Y, Li H, Jiang S, Fu D, Lu X, Lu M, et al. The glycolytic enzyme PFKFB3 drives kidney fibrosis through promoting histone lactylation-mediated NF-\u03baB family activation. Kidney Int. 2024;106(2):226\u201340.","journal-title":"Kidney Int"},{"issue":"28","key":"7350_CR81","doi-asserted-by":"publisher","first-page":"e2307216","DOI":"10.1002\/advs.202307216","volume":"11","author":"J Qiao","year":"2024","unstructured":"Qiao J, Tan Y, Liu H, Yang B, Zhang Q, Liu Q, et al. Histone H3K18 and ezrin lactylation promote renal dysfunction in sepsis-associated acute kidney injury. Adv Sci (Weinh). 2024;11(28):e2307216.","journal-title":"Adv Sci (Weinh)"},{"key":"7350_CR82","doi-asserted-by":"publisher","first-page":"111418","DOI":"10.1016\/j.cbi.2025.111418","volume":"408","author":"T Zheng","year":"2025","unstructured":"Zheng T, Gu YP, Wang JM, Huang TT, Gou LS, Liu YW. Lactate-triggered histone lactylation contributes to podocyte epithelial-mesenchymal transition in diabetic nephropathy in mice. Chem Biol Interact. 2025;408:111418.","journal-title":"Chem Biol Interact"},{"issue":"9","key":"7350_CR83","doi-asserted-by":"publisher","first-page":"882","DOI":"10.1038\/s42255-020-0267-9","volume":"2","author":"L Li","year":"2020","unstructured":"Li L, Chen K, Wang T, Wu Y, Xing G, Chen M, et al. Glis1 facilitates induction of pluripotency via an epigenome-metabolome-epigenome signalling cascade. Nat Metab. 2020;2(9):882\u201392.","journal-title":"Nat Metab"},{"issue":"11","key":"7350_CR84","doi-asserted-by":"publisher","first-page":"893","DOI":"10.1161\/CIRCRESAHA.122.320488","volume":"131","author":"N Wang","year":"2022","unstructured":"Wang N, Wang W, Wang X, Mang G, Chen J, Yan X, et al. Histone lactylation boosts reparative gene activation post-myocardial infarction. Circ Res. 2022;131(11):893\u2013908.","journal-title":"Circ Res"},{"issue":"1","key":"7350_CR85","doi-asserted-by":"publisher","first-page":"85","DOI":"10.1186\/s13059-021-02308-z","volume":"22","author":"J Yu","year":"2021","unstructured":"Yu J, Chai P, Xie M, Ge S, Ruan J, Fan X, et al. Histone lactylation drives oncogenesis by facilitating m(6)A reader protein YTHDF2 expression in ocular melanoma. Genome Biol. 2021;22(1):85.","journal-title":"Genome Biol"},{"issue":"11","key":"7350_CR86","doi-asserted-by":"publisher","first-page":"4797","DOI":"10.1172\/JCI122313","volume":"129","author":"S Kishi","year":"2019","unstructured":"Kishi S, Brooks CR, Taguchi K, Ichimura T, Mori Y, Akinfolarin A, et al. Proximal tubule atr regulates dna repair to prevent maladaptive renal injury responses. J. Clin. Invest. 2019;129(11):4797\u2013816.","journal-title":"J. Clin. Invest"},{"issue":"12","key":"7350_CR87","doi-asserted-by":"publisher","first-page":"2668","DOI":"10.2337\/db18-0124","volume":"67","author":"TA Alghamdi","year":"2018","unstructured":"Alghamdi TA, Batchu SN, Hadden MJ, Yerra VG, Liu Y, Bowskill BB, et al. Histone H3 serine 10 phosphorylation facilitates endothelial activation in diabetic kidney disease. Diabetes. 2018;67(12):2668\u201381.","journal-title":"Diabetes"},{"key":"7350_CR88","doi-asserted-by":"publisher","first-page":"103246","DOI":"10.1016\/j.redox.2024.103246","volume":"75","author":"X Zhang","year":"2024","unstructured":"Zhang X, Chen J, Lin R, Huang Y, Wang Z, Xu S, et al. Lactate drives epithelial-mesenchymal transition in diabetic kidney disease via the H3K14la\/KLF5 pathway. Redox Biol. 2024;75:103246.","journal-title":"Redox Biol"},{"issue":"8","key":"7350_CR89","doi-asserted-by":"publisher","first-page":"4500","DOI":"10.1093\/nar\/gkac259","volume":"50","author":"M Udugama","year":"2022","unstructured":"Udugama M, Vinod B, Chan FL, Hii L, Garvie A, Collas P, et al. Histone H3.3 phosphorylation promotes heterochromatin formation by inhibiting H3K9\/K36 histone demethylase. Nucleic Acids Res. 2022;50(8):4500\u201314.","journal-title":"Nucleic Acids Res"},{"issue":"5","key":"7350_CR90","doi-asserted-by":"publisher","first-page":"800","DOI":"10.1111\/j.1365-313X.2012.05029.x","volume":"71","author":"Q Dong","year":"2012","unstructured":"Dong Q, Han F. Phosphorylation of histone H2A is associated with centromere function and maintenance in meiosis. The Plant J. 2012;71(5):800\u201309.","journal-title":"The Plant J"},{"issue":"50","key":"7350_CR91","doi-asserted-by":"publisher","first-page":"39108","DOI":"10.1074\/jbc.M110.151753","volume":"285","author":"W Wen","year":"2010","unstructured":"Wen W, Zhu F, Zhang J, Keum YS, Zykova T, Yao K, et al. MST1 promotes apoptosis through phosphorylation of histone H2AX. J Biol Chem. 2010;285(50):39108\u201316.","journal-title":"J Biol Chem"},{"issue":"6796","key":"7350_CR92","doi-asserted-by":"publisher","first-page":"593","DOI":"10.1038\/35020506","volume":"406","author":"S Rea","year":"2000","unstructured":"Rea S, Eisenhaber F, O\u2019Carroll D, Strahl BD, Sun ZW, Schmid M, et al. Regulation of chromatin structure by site-specific histone H3 methyltransferases. Nature. 2000;406(6796):593\u201399.","journal-title":"Nature"},{"issue":"5595","key":"7350_CR93","doi-asserted-by":"publisher","first-page":"1039","DOI":"10.1126\/science.1076997","volume":"298","author":"R Cao","year":"2002","unstructured":"Cao R, Wang L, Wang H, Xia L, Erdjument-Bromage H, Tempst P, et al. Role of histone H3 lysine 27 methylation in Polycomb-group silencing. Science. 2002;298(5595):1039\u201343.","journal-title":"Science"},{"issue":"7","key":"7350_CR94","doi-asserted-by":"publisher","first-page":"941","DOI":"10.1016\/j.cell.2004.12.012","volume":"119","author":"Y Shi","year":"2004","unstructured":"Shi Y, Lan F, Matson C, Mulligan P, Whetstine JR, Cole PA, et al. Histone demethylation mediated by the nuclear amine oxidase homolog LSD1. Cell. 2004;119(7):941\u201353.","journal-title":"Cell"},{"issue":"8","key":"7350_CR95","doi-asserted-by":"publisher","first-page":"689","DOI":"10.1038\/nsmb1273","volume":"14","author":"JF Couture","year":"2007","unstructured":"Couture JF, Collazo E, Ortiz-Tello PA, Brunzelle JS, Trievel RC. Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase. Nat Struct Mol Biol. 2007;14(8):689\u201395.","journal-title":"Nat Struct Mol Biol"},{"key":"7350_CR96","doi-asserted-by":"crossref","unstructured":"Ogryzko S VV, Russanova RL, Howard V, Nakatani BH, Y. The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell. 1996;87(5):953\u201359.","DOI":"10.1016\/S0092-8674(00)82001-2"},{"key":"7350_CR97","doi-asserted-by":"crossref","unstructured":"Lee SY, Lee SH, Choi NH, Kim JY, Kweon JH, Miller KM, et al. PCAF promotes R-loop resolution via histone acetylation. Nucleic Acids Res. 2024;52(15):8643\u201360.","DOI":"10.1093\/nar\/gkae558"},{"key":"7350_CR98","doi-asserted-by":"crossref","unstructured":"Gregoretti L IV, Goodson YM, HV. Molecular evolution of the histone deacetylase family: functional implications of phylogenetic analysis. J Mol Biol. 2004;338(1):17\u201331.","DOI":"10.1016\/j.jmb.2004.02.006"},{"key":"7350_CR99","doi-asserted-by":"crossref","unstructured":"Hendzel MJ, Wei Y, Mancini MA, Van Hooser A, Ranalli T, Brinkley BR, et al. Mitosis-specific phosphorylation of histone H3 initiates primarily within pericentromeric heterochromatin during G2 and spreads in an ordered fashion coincident with mitotic chromosome condensation. Chromosoma. 1997;106(6):348\u201360.","DOI":"10.1007\/s004120050256"},{"key":"7350_CR100","doi-asserted-by":"crossref","unstructured":"Zhang D, Tang Z, Huang H, Zhou G, Cui C, Weng Y, et al. Metabolic regulation of gene expression by histone lactylation. Nature. 2019;574(7779):575\u201380.","DOI":"10.1038\/s41586-019-1678-1"},{"key":"7350_CR101","doi-asserted-by":"crossref","unstructured":"Rho H, Hay N. Protein lactylation in cancer: mechanisms and potential therapeutic implications. Exp Mol Med. 2025;57(3):545\u201353.","DOI":"10.1038\/s12276-025-01410-7"},{"key":"7350_CR102","doi-asserted-by":"crossref","unstructured":"Zhou X, Chen H, Hu Y, Ma X, Li J, Shi Y, et al. Enhancer of zeste homolog 2 promotes renal fibrosis after acute kidney injury by inducing epithelial-mesenchymal transition and activation of M2 macrophage polarization. Cell Death Dis. 2023;14(4):253.","DOI":"10.1038\/s41419-023-05782-4"},{"key":"7350_CR103","doi-asserted-by":"crossref","unstructured":"Zhang C, Guan Y, Zou J, Yang X, Bayliss G, Zhuang S. Histone methyltransferase MLL1 drives renal tubular cell apoptosis by p53-dependent repression of E-cadherin during cisplatin-induced acute kidney injury. Cell Death Dis. 2022;13(9):770.","DOI":"10.1038\/s41419-022-05104-0"},{"key":"7350_CR104","doi-asserted-by":"crossref","unstructured":"Liu YF, Li F, Xu CY, Chen Y, Tu WP, Huang C. SETDB1 recruits CBX3 to regulate the SIRT4\/PTEN axis, inhibiting autophagy and promoting ischemia-reperfusion-induced kidney injury. Faseb J. 2025;39(7):e70509.","DOI":"10.1096\/fj.202403024R"},{"key":"7350_CR105","doi-asserted-by":"crossref","unstructured":"Yu C, Tang J, Yu J, Wang Y, Liu N, Dong Z, et al. JMJD3 activation contributes to renal protection and regeneration following acute kidney injury in mice. Faseb J. 2024;38(7):e23583.","DOI":"10.1096\/fj.202300681R"},{"key":"7350_CR106","doi-asserted-by":"crossref","unstructured":"Ma T, Huang C, Xu Q, Yang Y, Liu Y, Meng X, et al. Suppression of BMP-7 by histone deacetylase 2 promoted apoptosis of renal tubular epithelial cells in acute kidney injury. Cell Death Dis. 2017;8(10):e3139.","DOI":"10.1038\/cddis.2017.552"},{"key":"7350_CR107","doi-asserted-by":"crossref","unstructured":"Xu Z, Jia K, Wang H, Gao F, Zhao S, Li F, et al. METTL14-regulated PI3K\/Akt signaling pathway via pten affects HDAC5-mediated epithelial-mesenchymal transition of renal tubular cells in diabetic kidney disease. Cell Death Dis. 2021;12(1):32.","DOI":"10.1038\/s41419-020-03312-0"},{"key":"7350_CR108","doi-asserted-by":"crossref","unstructured":"Conserva F, Gesualdo L, Papale M. A systems biology overview on human diabetic nephropathy: from genetic susceptibility to post-transcriptional and post-translational modifications. J Diabetes Res. 2016;2016:7934504.","DOI":"10.1155\/2016\/7934504"},{"key":"7350_CR109","doi-asserted-by":"crossref","unstructured":"Huang J, Wan D, Li J, Chen H, Huang K, Zheng L. Histone acetyltransferase PCAF regulates inflammatory molecules in the development of renal injury. Epigenetics. 2015;10(1):62\u201372.","DOI":"10.4161\/15592294.2014.990780"},{"key":"7350_CR110","doi-asserted-by":"crossref","unstructured":"Chen J, He J, Wang X, Bai L, Yang X, Chen J, et al. Glis1 inhibits rtec cellular senescence and renal fibrosis by downregulating histone lactylation in DKD. Life Sci. 2025;361:123293.","DOI":"10.1016\/j.lfs.2024.123293"},{"key":"7350_CR111","doi-asserted-by":"crossref","unstructured":"Jiang W, Yuan X, Zhu H, He C, Ge C, Tang Q, et al. Inhibition of histone H3K27 acetylation orchestrates interleukin-9-mediated and plays an Anti-inflammatory role in cisplatin-induced acute kidney injury. Front Immunol. 2020;11:231.","DOI":"10.3389\/fimmu.2020.00231"},{"key":"7350_CR112","doi-asserted-by":"crossref","unstructured":"Wang Y, Jiao B, Hu Z, Wang Y. Critical role of histone deacetylase 3 in the regulation of kidney inflammation and fibrosis. Kidney Int. 2024;105(4):775\u201390.","DOI":"10.1016\/j.kint.2024.01.010"},{"key":"7350_CR113","doi-asserted-by":"crossref","unstructured":"Wu WP, Tsai YG, Lin TY, Wu MJ, Lin CY. The attenuation of renal fibrosis by histone deacetylase inhibitors is associated with the plasticity of FOXP3(+)IL-17(+) T cells. BMC Nephrol. 2017;18(1):225.","DOI":"10.1186\/s12882-017-0630-6"},{"key":"7350_CR114","doi-asserted-by":"crossref","unstructured":"Pang M, Ma L, Liu N, Ponnusamy M, Zhao TC, Yan H, et al. Histone deacetylase 1\/2 mediates proliferation of renal interstitial fibroblasts and expression of cell cycle proteins. J Cell Biochem. 2011;112(8):2138\u201348.","DOI":"10.1002\/jcb.23135"},{"key":"7350_CR115","doi-asserted-by":"crossref","unstructured":"Liu N, He S, Ma L, Ponnusamy M, Tang J, Tolbert E, et al. Blocking the class I histone deacetylase ameliorates renal fibrosis and inhibits renal fibroblast activation via modulating TGF-beta and EGFR signaling. PLoS One. 2013;8(1):e54001.","DOI":"10.1371\/journal.pone.0054001"},{"key":"7350_CR116","doi-asserted-by":"crossref","unstructured":"He X, Sun T, Zhang P, Xia Z, Gao C, Ren H, et al. Selective inhibition of histone deacetylase class IIa with MC1568 ameliorates podocyte injury. Front Med (Lausanne). 2022;9:848938.","DOI":"10.3389\/fmed.2022.848938"},{"key":"7350_CR117","unstructured":"Hou C, Ouyang L, Wang Y, Zhou Z. Relationship between histone acetylation modification in spleen CD4+T cells and diabetic nephropathy of nonobese diabetic mice. Zhonghua Yi Xue Za Zhi. 2015;95(14):1061\u201365."},{"key":"7350_CR118","doi-asserted-by":"crossref","unstructured":"Zeisberg M, Kalluri R. Physiology of the renal interstitium. Clin J Am Soc Nephrol. 2015;10(10):1831\u201340.","DOI":"10.2215\/CJN.00640114"},{"key":"7350_CR119","doi-asserted-by":"crossref","unstructured":"Tang J, Yan H, Zhuang S. Histone deacetylases as targets for treatment of multiple diseases. Clin Sci (lond). 2013;124(11):651\u201362.","DOI":"10.1042\/CS20120504"},{"key":"7350_CR120","doi-asserted-by":"publisher","first-page":"117487","DOI":"10.1016\/j.cca.2023.117487","volume":"548","author":"V Singh","year":"2023","unstructured":"Singh V, Kaur R, Kumari P, Pasricha C, Singh R. ICAM-1 and VCAM-1: gatekeepers in various inflammatory and cardiovascular disorders. Clin Chim Acta. 2023;548:117487.","journal-title":"Clin Chim Acta"},{"key":"7350_CR121","doi-asserted-by":"publisher","first-page":"569322","DOI":"10.3389\/fphys.2020.569322","volume":"11","author":"L Sheng","year":"2020","unstructured":"Sheng L, Zhuang S. New insights into the role and mechanism of partial epithelial-mesenchymal transition in kidney fibrosis. Front Physiol. 2020;11:569322.","journal-title":"Front Physiol"},{"issue":"6","key":"7350_CR122","doi-asserted-by":"publisher","first-page":"1221","DOI":"10.1016\/j.kint.2016.01.012","volume":"89","author":"M Nagata","year":"2016","unstructured":"Nagata M. Podocyte injury and its consequences. Kidney Int. 2016;89(6):1221\u201330.","journal-title":"Kidney Int"},{"issue":"1","key":"7350_CR123","doi-asserted-by":"publisher","first-page":"1930","DOI":"10.1038\/s41467-019-09982-5","volume":"10","author":"HS Kaya-Okur","year":"2019","unstructured":"Kaya-Okur HS, Wu SJ, Codomo CA, Pledger ES, Bryson TD, Henikoff JG, et al. CUT&Tag for efficient epigenomic profiling of small samples and single cells. Nat Commun. 2019;10(1):1930.","journal-title":"Nat Commun"},{"issue":"1\u20132","key":"7350_CR124","doi-asserted-by":"publisher","first-page":"361","DOI":"10.1016\/j.cell.2018.11.022","volume":"176","author":"AJ Rubin","year":"2019","unstructured":"Rubin AJ, Parker KR, Satpathy AT, Qi Y, Wu B, Ong AJ, et al. Coupled single-cell CRISPR screening and epigenomic profiling reveals causal gene regulatory networks. Cell. 2019;176(1\u20132):361\u201376.e17.","journal-title":"Cell"},{"issue":"2","key":"7350_CR125","doi-asserted-by":"publisher","first-page":"135","DOI":"10.5306\/wjco.v7.i2.135","volume":"7","author":"I Marchesi","year":"2016","unstructured":"Marchesi I, Bagella L. Targeting enhancer of zeste homolog 2 as a promising strategy for cancer treatment. World J Clin Oncol. 2016;7(2):135\u201348.","journal-title":"World J Clin Oncol"},{"issue":"7427","key":"7350_CR126","doi-asserted-by":"publisher","first-page":"108","DOI":"10.1038\/nature11606","volume":"492","author":"MT McCabe","year":"2012","unstructured":"McCabe MT, Ott HM, Ganji G, Korenchuk S, Thompson C, Van Aller GS, et al. EZH2 inhibition as a therapeutic strategy for lymphoma with EZH2-activating mutations. Nature. 2012;492(7427):108\u201312.","journal-title":"Nature"},{"issue":"4","key":"7350_CR127","doi-asserted-by":"publisher","first-page":"842","DOI":"10.1158\/1535-7163.MCT-13-0773","volume":"13","author":"SK Knutson","year":"2014","unstructured":"Knutson SK, Kawano S, Minoshima Y, Warholic NM, Huang KC, Xiao Y, et al. Selective inhibition of EZH2 by EPZ-6438 leads to potent antitumor activity in EZH2-mutant non-hodgkin lymphoma. Mol Cancer Ther. 2014;13(4):842\u201354.","journal-title":"Mol Cancer Ther"},{"issue":"2","key":"7350_CR128","doi-asserted-by":"publisher","first-page":"158","DOI":"10.6004\/jadpro.2022.13.2.7","volume":"13","author":"R Straining","year":"2022","unstructured":"Straining R, Eighmy WT. EZH2 inhibitor. J Adv Pract Oncol. 2022;13(2):158\u201363.","journal-title":"J Adv Pract Oncol"},{"key":"7350_CR129","doi-asserted-by":"crossref","unstructured":"Sun F, Lee L, Zhang Z, Wang X, Yu Q, Duan X, et al. Preclinical pharmacokinetic studies of 3-deazaneplanocin a, a potent epigenetic anticancer agent, and its human pharmacokinetic prediction using GastroPlus\u2122. Eur J Pharm Sci. 2015;77:290\u2013302.","DOI":"10.1016\/j.ejps.2015.06.021"},{"key":"7350_CR130","doi-asserted-by":"crossref","unstructured":"Zhou X, Zang X, Ponnusamy M, Masucci MV, Tolbert E, Gong R, et al. Enhancer of zeste homolog 2 inhibition attenuates renal fibrosis by maintaining Smad7 and phosphatase and tensin homolog expression. J Am Soc Nephrol. 2016;27(7):2092\u2013108.","DOI":"10.1681\/ASN.2015040457"},{"key":"7350_CR131","doi-asserted-by":"crossref","unstructured":"Gounder M, Sch\u00f6ffski P, Jones RL, Agulnik M, Cote GM, Villalobos VM, et al. Tazemetostat in advanced epithelioid sarcoma with loss of INI1\/SMARCB1: an international, open-label, phase 2 basket study. The Lancet Oncol. 2020;21(11):1423\u201332.","DOI":"10.1016\/S1470-2045(20)30451-4"},{"key":"7350_CR132","doi-asserted-by":"crossref","unstructured":"Ryan QC, Headlee D, Acharya M, Sparreboom A, Trepel JB, Ye J, et al. Phase I and pharmacokinetic study of MS-275, a histone deacetylase inhibitor, in patients with advanced and refractory solid tumors or lymphoma. J Clin Oncol. 2005;23(17):3912\u201322.","DOI":"10.1200\/JCO.2005.02.188"},{"key":"7350_CR133","doi-asserted-by":"crossref","unstructured":"Sanderson L, Taylor GW, Aboagye EO, Alao JP, Latigo JR, Coombes RC, et al. Plasma pharmacokinetics and metabolism of the histone deacetylase inhibitor trichostatin a after intraperitoneal administration to mice. Drug Metab Dispos. 2004;32(10):1132\u201338.","DOI":"10.1124\/dmd.104.000638"},{"key":"7350_CR134","doi-asserted-by":"crossref","unstructured":"Teixeira-da-Silva P, P\u00e9rez-Blanco JS, Santos-Buelga D, Otero MJ, Garc\u00eda MJ. Population pharmacokinetics of valproic acid in pediatric and adult caucasian patients. Pharmaceutics. 2022;14(4).","DOI":"10.3390\/pharmaceutics14040811"},{"key":"7350_CR135","doi-asserted-by":"crossref","unstructured":"Miller KD, Pniewski K, Perry CE, Papp SB, Shaffer JD, Velasco-Silva JN, et al. Targeting ACSS2 with a transition-state mimetic inhibits triple-negative breast cancer growth. Cancer Res. 2021;81(5):1252\u201364.","DOI":"10.1158\/0008-5472.CAN-20-1847"},{"key":"7350_CR136","doi-asserted-by":"crossref","unstructured":"Wang Y, Qu C, Liu T, Wang C. PFKFB3 inhibitors as potential anticancer agents: mechanisms of action, current developments, and structure-activity relationships. Eur J Med Chem. 2020;203:112612.","DOI":"10.1016\/j.ejmech.2020.112612"},{"key":"7350_CR137","doi-asserted-by":"crossref","unstructured":"Altinoz MA, Ozpinar A. Oxamate targeting aggressive cancers with special emphasis to brain tumors. Biomed Pharmacother. 2022;147:112686.","DOI":"10.1016\/j.biopha.2022.112686"},{"key":"7350_CR138","doi-asserted-by":"crossref","unstructured":"Li Y, Seto E. HDACs and HDAC inhibitors in cancer development and therapy. Cold Spring Harb Perspect Med. 2016;6(10).","DOI":"10.1101\/cshperspect.a026831"},{"key":"7350_CR139","doi-asserted-by":"crossref","unstructured":"Pili R, Quinn DI, Hammers HJ, Monk P, George S, Dorff TB, et al. Immunomodulation by entinostat in renal cell carcinoma patients receiving high-dose interleukin 2: a multicenter, single-arm, phase I\/II trial (NCI-CTEP#7870). Clin Cancer Res. 2017;23(23):7199\u2013208.","DOI":"10.1158\/1078-0432.CCR-17-1178"},{"key":"7350_CR140","doi-asserted-by":"crossref","unstructured":"Pili R, Quinn DI, Hammers HJ, Monk P, George S, Dorff TB, et al. Immunomodulation by entinostat in renal cell carcinoma patients receiving high-dose interleukin 2: a multicenter, single-arm, phase I\/II trial (NCI-CTEP#7870). Clin Cancer Res. 2017;23(23):7199\u2013208.","DOI":"10.1158\/1078-0432.CCR-17-1178"},{"key":"7350_CR141","doi-asserted-by":"crossref","unstructured":"Porter NJ, Christianson DW. Structure, mechanism, and inhibition of the zinc-dependent histone deacetylases. Curr Opin Struct Biol. 2019;59:9\u201318.","DOI":"10.1016\/j.sbi.2019.01.004"},{"key":"7350_CR142","doi-asserted-by":"crossref","unstructured":"Phiel CJ, Zhang F, Huang EY, Guenther MG, Lazar MA, Klein PS. Histone deacetylase is a direct target of valproic acid, a potent anticonvulsant, mood stabilizer, and teratogen. J Biol Chem. 2001;276(39):36734\u201341.","DOI":"10.1074\/jbc.M101287200"},{"key":"7350_CR143","doi-asserted-by":"crossref","unstructured":"Esquea EM, Ciraku L, Young RG, Merzy J, Talarico AN, Ahmed NN, et al. Selective and brain-penetrant ACSS2 inhibitors target breast cancer brain metastatic cells. Front Pharmacol. 2024;15:1394685.","DOI":"10.3389\/fphar.2024.1394685"}],"container-title":["Journal of Translational Medicine"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1186\/s12967-025-07350-0.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1186\/s12967-025-07350-0\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1186\/s12967-025-07350-0.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,11,25]],"date-time":"2025-11-25T13:05:39Z","timestamp":1764075939000},"score":1,"resource":{"primary":{"URL":"https:\/\/translational-medicine.biomedcentral.com\/articles\/10.1186\/s12967-025-07350-0"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,11,25]]},"references-count":143,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2025,12]]}},"alternative-id":["7350"],"URL":"https:\/\/doi.org\/10.1186\/s12967-025-07350-0","relation":{},"ISSN":["1479-5876"],"issn-type":[{"value":"1479-5876","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,11,25]]},"assertion":[{"value":"28 August 2025","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"18 October 2025","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"25 November 2025","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"Not applicable.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Ethics approval and consent to participate"}},{"value":"Not applicable.","order":3,"name":"Ethics","group":{"name":"EthicsHeading","label":"Consent for publication"}},{"value":"The authors declare that they have no competing interests.","order":4,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}],"article-number":"1346"}}